Dermaseptin, a peptide isolated from frog skin, exhibits potent antimicrobial activity against bacteria, fungi and protozoa.

Dermaseptin is a water-soluble, thermostable, and nonhemolytic peptide endowed with highly potent antimicrobial activity against pathogenic fungi at micromolar concentration. Circular dichroism spectra of dermaseptin in hydrophobic media indicated 80% alpha-helical conformation, and predictions of secondary structure suggested that dermaseptin can be configured as an amphiphatic alpha-helix spanning over residues 1-27, a structure that perturbs membrane functions regulating water flux[1]. Dermaseptin exerts a lytic action upon bacteria, protozoa, yeasts, and filamentous fungi at micromolar concentrations. Molecular elements responsible for the exceptional antimicrobial potency of dermaseptin are to be traced to the NH2-terminal alpha-helical amphipathic segment spanning residues 1-18 of the molecule[1].

[1]. Mor A, et al. Isolation, amino acid sequence, and synthesis of dermaseptin, a novel antimicrobial peptide of amphibian skin. Biochemistry. 1991 Sep 10;30(36):8824-30. [2]. Mor A, et al. The NH2-terminal alpha-helical domain 1-18 of dermaseptin is responsible for antimicrobial activity. J Biol Chem. 1994 Jan 21;269(3):1934-9.